Piranoza dehidrogenaza (akceptor)
Piranoza dehidrogenaza (akceptor) | |||||||||
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Identifikatori | |||||||||
EC broj | 1.1.99.29 | ||||||||
CAS broj | 190606-21-4 | ||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Piranoza dehidrogenaza (akceptor) (EC 1.1.99.29, piranozna dehidrogenaza, piranozo-hinonska oksidoreduktaza, hinon-zavisna piranozna dehidrogenaza, PDH) je enzim sa sistematskim imenom piranoza:akceptor oksidoreduktaza.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
- (1) piranoza + akceptor piranoz-2-uloza (ili piranoz-3-uloza ili piranoz-2,3-diuloza) + redukovani akceptor
- (2) piranozid + akceptor piranozid-3-uloza (ili piranozid-3,4-diuloza) + redukovani akceptor
Za rad ovog enzima je neophodan FAD. Brojne aldoze i ketoze u piranoznoj formi, kao i glikozidi, gluko-oligosaharidi, saharoza i laktoza mogu da deluju kao donori. 1,4-Benzohinon ili fericenijumski jon (ferocen oksidovan uklanjanjem jednog elektrona) može da služi kao akceptor. Za razliku od EC 1.1.3.10, piranozna oksidaza, ovaj fungalni enzim ne formira interakcije sa O2 i ispoljava ekstremno široku supstratnu toleranciju sa varijabilnom regioselektivnošću (C-3, C-2 ili C-3 + C-2 ili C-3 + C-4) za (di)oksidaciju različitih šećera.
Reference[uredi | uredi kod]
- ↑ Volc, J., Kubátová, E., Wood, D. and Daniel, G. (1997). „Pyranose 2-dehydrogenase, a novel sugar oxidoreductase from the basidiomycete fungus Agaricus bisporus”. Arch. Microbiol. 167: 119-125. PMID 9042751.
- ↑ Volc, J., Sedmera, P., Halada, P., Pøikyrlová, V. and Daniel, G. (1998). „C-2 and C-3 oxidation of D-Glc, and C-2 oxidation of D-Gal by pyranose dehydrogenase from Agaricus bisporus”. Carbohydr. Res. 310: 151-156.
- ↑ Volc, J., Sedmera, P., Halada, P., Pøikyrlová, V. and Haltrich, D. (2000). „Double oxidation of D-xylose to D-glycero-pentos-2,3-diulose (2,3-diketo-D-xylose) by pyranose dehydrogenase from the mushroom Agaricus bisporus”. Carbohydr. Res. 329: 219-225. PMID 11086703.
- ↑ Volc, J., Kubátová, E., Daniel, G., Sedmera, P. and Haltrich, D. (2001). „Screening of basidiomycete fungi for the quinone-dependent sugar C-2/C-3 oxidoreductase, pyranose dehydrogenase, and properties of the enzyme from Macrolepiota rhacodes”. Arch. Microbiol. 176: 178-186. PMID 11511865.
- ↑ Volc, J., Sedmera, P., Halada, P., Daniel, G., Pøikyrlová, V. and Haltrich, D. (2002). „C-3 oxidation of non-reducing sugars by a fungal pyranose dehydrogenase: spectral characterization”. J. Mol. Catal., B Enzym. 17: 91-100.
Literatura[uredi | uredi kod]
- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
- Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.